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Volumn 2, Issue 9, 2016, Pages 519-531

Cadherins Glycans in Cancer: Sweet Players in a Bitter Process

Author keywords

cancer progression; classical cadherin; glycosylation; invasion; metastasis; N glycosylation; O glycosylation

Indexed keywords

CADHERIN; GLYCAN; TUMOR MARKER; POLYSACCHARIDE;

EID: 84989821862     PISSN: 24058033     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.trecan.2016.08.003     Document Type: Review
Times cited : (32)

References (149)
  • 1
    • 84926436140 scopus 로고    scopus 로고
    • Tissue invasion and metastasis: molecular, biological and clinical perspectives
    • 1 Jiang, W.G., et al. Tissue invasion and metastasis: molecular, biological and clinical perspectives. Semin Cancer Biol. 35:Suppl. (2015), S244–S275.
    • (2015) Semin Cancer Biol. , vol.35 , pp. S244-S275
    • Jiang, W.G.1
  • 2
    • 84940449986 scopus 로고    scopus 로고
    • Glycosylation in cancer: mechanisms and clinical implications
    • 2 Pinho, S.S., Reis, C.A., Glycosylation in cancer: mechanisms and clinical implications. Nat. Rev. Cancer 15 (2015), 540–555.
    • (2015) Nat. Rev. Cancer , vol.15 , pp. 540-555
    • Pinho, S.S.1    Reis, C.A.2
  • 3
    • 84925352315 scopus 로고    scopus 로고
    • Cadherins in tissue architecture and disease
    • 3 Vestweber, D., Cadherins in tissue architecture and disease. J. Mol. Med. 93 (2015), 5–11.
    • (2015) J. Mol. Med. , vol.93 , pp. 5-11
    • Vestweber, D.1
  • 4
    • 79955642014 scopus 로고    scopus 로고
    • Tissue organization by cadherin adhesion molecules: dynamic molecular and cellular mechanisms of morphogenetic regulation
    • 4 Niessen, C.M., et al. Tissue organization by cadherin adhesion molecules: dynamic molecular and cellular mechanisms of morphogenetic regulation. Physiol. Rev. 91 (2011), 691–731.
    • (2011) Physiol. Rev. , vol.91 , pp. 691-731
    • Niessen, C.M.1
  • 5
    • 84937137949 scopus 로고    scopus 로고
    • Jack of all trades: functional modularity in the adherens junction
    • 5 Padmanabhan, A., et al. Jack of all trades: functional modularity in the adherens junction. Curr. Opin. Cell Biol. 36 (2015), 32–40.
    • (2015) Curr. Opin. Cell Biol. , vol.36 , pp. 32-40
    • Padmanabhan, A.1
  • 6
    • 84950158923 scopus 로고    scopus 로고
    • Towards a dynamic understanding of cadherin-based mechanobiology
    • 6 Hoffman, B.D., Yap, A.S., Towards a dynamic understanding of cadherin-based mechanobiology. Trends Cell Biol. 25 (2015), 803–814.
    • (2015) Trends Cell Biol. , vol.25 , pp. 803-814
    • Hoffman, B.D.1    Yap, A.S.2
  • 8
    • 84875279977 scopus 로고    scopus 로고
    • Cadherins and epithelial-to-mesenchymal transition
    • 8 Gheldof, A., Berx, G., Cadherins and epithelial-to-mesenchymal transition. Prog. Mol. Biol. Transl. Sci. 116 (2013), 317–336.
    • (2013) Prog. Mol. Biol. Transl. Sci. , vol.116 , pp. 317-336
    • Gheldof, A.1    Berx, G.2
  • 9
    • 84894520335 scopus 로고    scopus 로고
    • Beyond E-cadherin: roles of other cadherin superfamily members in cancer
    • 9 van Roy, F., Beyond E-cadherin: roles of other cadherin superfamily members in cancer. Nat. Rev. Cancer 14 (2014), 121–134.
    • (2014) Nat. Rev. Cancer , vol.14 , pp. 121-134
    • van Roy, F.1
  • 10
    • 77953879928 scopus 로고    scopus 로고
    • Involvement of members of the cadherin superfamily in cancer
    • 10 Berx, G., van Roy, F., Involvement of members of the cadherin superfamily in cancer. Cold Spring Harb. Perspect. Biol., 1, 2009, a003129.
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1 , pp. a003129
    • Berx, G.1    van Roy, F.2
  • 11
    • 57349114162 scopus 로고    scopus 로고
    • The cell–cell adhesion molecule E-cadherin
    • 11 van Roy, F., Berx, G., The cell–cell adhesion molecule E-cadherin. Cell Mol. Life Sci. 65 (2008), 3756–3788.
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 3756-3788
    • van Roy, F.1    Berx, G.2
  • 12
    • 80052080271 scopus 로고    scopus 로고
    • Loss of heterozygosity of tumor suppressor genes (p16, Rb, E-cadherin, p53) in hypopharynx squamous cell carcinoma
    • 12 Sang-Hyuk Lee, S.H., et al. Loss of heterozygosity of tumor suppressor genes (p16, Rb, E-cadherin, p53) in hypopharynx squamous cell carcinoma. Otolaryngol. Head Neck Surg. 145 (2011), 64–70.
    • (2011) Otolaryngol. Head Neck Surg. , vol.145 , pp. 64-70
    • Sang-Hyuk Lee, S.H.1
  • 13
    • 0038784580 scopus 로고    scopus 로고
    • Frequent E-cadherin gene inactivation by loss of heterozygosity in pleomorphic lobular carcinoma of the breast
    • 13 Palacios, J., et al. Frequent E-cadherin gene inactivation by loss of heterozygosity in pleomorphic lobular carcinoma of the breast. Mod. Pathol. 16 (2003), 674–678.
    • (2003) Mod. Pathol. , vol.16 , pp. 674-678
    • Palacios, J.1
  • 14
    • 84930650698 scopus 로고    scopus 로고
    • Hereditary diffuse gastric cancer: updated clinical guidelines with an emphasis on germline CDH1 mutation carriers
    • 14 van der Post, R.S., et al. Hereditary diffuse gastric cancer: updated clinical guidelines with an emphasis on germline CDH1 mutation carriers. J. Med. Genet. 52 (2015), 361–374.
    • (2015) J. Med. Genet. , vol.52 , pp. 361-374
    • van der Post, R.S.1
  • 15
    • 84914121710 scopus 로고    scopus 로고
    • E-Cadherin germline mutation carriers: clinical management and genetic implications
    • 15 Corso, G., et al. E-Cadherin germline mutation carriers: clinical management and genetic implications. Cancer Metastasis Rev. 33 (2014), 1081–1094.
    • (2014) Cancer Metastasis Rev. , vol.33 , pp. 1081-1094
    • Corso, G.1
  • 16
    • 84919880745 scopus 로고    scopus 로고
    • Downregulation of E-cadherin expression in breast cancer by promoter hypermethylation and its relation with progression and prognosis of tumor
    • 16 Shargh, S.A., et al. Downregulation of E-cadherin expression in breast cancer by promoter hypermethylation and its relation with progression and prognosis of tumor. Med. Oncol., 31, 2014, 250.
    • (2014) Med. Oncol. , vol.31 , pp. 250
    • Shargh, S.A.1
  • 17
    • 34247550919 scopus 로고    scopus 로고
    • CDH1 promoter hypermethylation and E-cadherin protein expression in infiltrating breast cancer
    • 17 Caldeira, J.R., et al. CDH1 promoter hypermethylation and E-cadherin protein expression in infiltrating breast cancer. BMC Cancer, 6, 2006, 48.
    • (2006) BMC Cancer , vol.6 , pp. 48
    • Caldeira, J.R.1
  • 18
    • 83755220911 scopus 로고    scopus 로고
    • E-Cadherin is transcriptionally activated via suppression of ZEB1 transcriptional repressor by small RNA-mediated gene silencing
    • 18 Mazda, M., et al. E-Cadherin is transcriptionally activated via suppression of ZEB1 transcriptional repressor by small RNA-mediated gene silencing. PLoS ONE, 6, 2011, e28688.
    • (2011) PLoS ONE , vol.6 , pp. e28688
    • Mazda, M.1
  • 19
    • 84903715184 scopus 로고    scopus 로고
    • Retrograde flow of cadherins in collective cell migration
    • 19 Hirata, E., et al. Retrograde flow of cadherins in collective cell migration. Nat. Cell Biol. 16 (2014), 621–623.
    • (2014) Nat. Cell Biol. , vol.16 , pp. 621-623
    • Hirata, E.1
  • 21
    • 84953775166 scopus 로고    scopus 로고
    • Beyond a tumor suppressor: soluble E-cadherin promotes the progression of cancer
    • 21 Hu, Q.P., et al. Beyond a tumor suppressor: soluble E-cadherin promotes the progression of cancer. Int. J. Cancer 138 (2016), 2804–2812.
    • (2016) Int. J. Cancer , vol.138 , pp. 2804-2812
    • Hu, Q.P.1
  • 22
    • 84875753760 scopus 로고    scopus 로고
    • Somatic mutations and deletions of the E-cadherin gene predict poor survival of patients with gastric cancer
    • 22 Corso, G., et al. Somatic mutations and deletions of the E-cadherin gene predict poor survival of patients with gastric cancer. J. Clin. Oncol. 31 (2013), 868–875.
    • (2013) J. Clin. Oncol. , vol.31 , pp. 868-875
    • Corso, G.1
  • 23
    • 84886951831 scopus 로고    scopus 로고
    • Gastric cancer: adding glycosylation to the equation
    • 23 Pinho, S.S., et al. Gastric cancer: adding glycosylation to the equation. Trends Mol. Med. 19 (2013), 664–676.
    • (2013) Trends Mol. Med. , vol.19 , pp. 664-676
    • Pinho, S.S.1
  • 24
    • 42449143890 scopus 로고    scopus 로고
    • Branched N-glycans regulate the biological functions of integrins and cadherins
    • 24 Zhao, Y., et al. Branched N-glycans regulate the biological functions of integrins and cadherins. FEBS J. 275 (2008), 1939–1948.
    • (2008) FEBS J. , vol.275 , pp. 1939-1948
    • Zhao, Y.1
  • 25
    • 84862728161 scopus 로고    scopus 로고
    • Vertebrate protein glycosylation: diversity, synthesis and function
    • 25 Moremen, K.W., et al. Vertebrate protein glycosylation: diversity, synthesis and function. Nat. Rev. Mol. Cell Biol. 13 (2012), 448–462.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 448-462
    • Moremen, K.W.1
  • 26
    • 84955565229 scopus 로고    scopus 로고
    • Cracking the glycome encoder: signaling, trafficking, and glycosylation
    • 26 Bard, F., Chia, J., Cracking the glycome encoder: signaling, trafficking, and glycosylation. Trends Cell Biol. 26 (2016), 379–388.
    • (2016) Trends Cell Biol. , vol.26 , pp. 379-388
    • Bard, F.1    Chia, J.2
  • 27
    • 84874911605 scopus 로고    scopus 로고
    • Thematic minireview series on glycobiology and extracellular matrices: glycan functions pervade biology at all levels
    • 6903-6903
    • 27 Hart, G.W., Thematic minireview series on glycobiology and extracellular matrices: glycan functions pervade biology at all levels. J. Biol. Chem., 288, 2013 6903-6903.
    • (2013) J. Biol. Chem. , vol.288
    • Hart, G.W.1
  • 28
    • 84973310291 scopus 로고    scopus 로고
    • Hallmarks of glycosylation in cancer
    • Published online March 17, 2016
    • 28 Munkley, J., Elliott, D.J., Hallmarks of glycosylation in cancer. Oncotarget, 2016, 10.18632/oncotarget.8155 Published online March 17, 2016.
    • (2016) Oncotarget
    • Munkley, J.1    Elliott, D.J.2
  • 29
    • 84921930328 scopus 로고    scopus 로고
    • Protein glycosylation in cancer
    • 29 Stowell, S.R., et al. Protein glycosylation in cancer. Annu. Rev. Pathol. 10 (2015), 473–510.
    • (2015) Annu. Rev. Pathol. , vol.10 , pp. 473-510
    • Stowell, S.R.1
  • 30
    • 77950410995 scopus 로고    scopus 로고
    • Alterations in glycosylation as biomarkers for cancer detection
    • 30 Reis, C.A., et al. Alterations in glycosylation as biomarkers for cancer detection. J. Clin. Pathol. 63 (2010), 322–329.
    • (2010) J. Clin. Pathol. , vol.63 , pp. 322-329
    • Reis, C.A.1
  • 31
    • 84962877719 scopus 로고    scopus 로고
    • N-Linked glycosylation and homeostasis of the endoplasmic reticulum
    • 31 Cherepanova, N., et al. N-Linked glycosylation and homeostasis of the endoplasmic reticulum. Curr. Opin. Cell Biol. 41 (2016), 57–65.
    • (2016) Curr. Opin. Cell Biol. , vol.41 , pp. 57-65
    • Cherepanova, N.1
  • 32
    • 46149089907 scopus 로고    scopus 로고
    • Effect of glycosylation on protein folding: a close look at thermodynamic stabilization
    • 32 Shental-Bechor, D., Levy, Y., Effect of glycosylation on protein folding: a close look at thermodynamic stabilization. Proc. Natl. Acad. Sci. U.S.A. 105 (2008), 8256–8261.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 8256-8261
    • Shental-Bechor, D.1    Levy, Y.2
  • 33
    • 84948075024 scopus 로고    scopus 로고
    • Glycosylation-directed quality control of protein folding
    • 33 Xu, C., Ng, D.T.W., Glycosylation-directed quality control of protein folding. Nat. Rev. Mol. Cell Biol. 16 (2015), 742–752.
    • (2015) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 742-752
    • Xu, C.1    Ng, D.T.W.2
  • 34
    • 84924370879 scopus 로고    scopus 로고
    • Effects of N-glycosylation on protein conformation and dynamics: Protein Data Bank analysis and molecular dynamics simulation study
    • 34 Lee, H.S., et al. Effects of N-glycosylation on protein conformation and dynamics: Protein Data Bank analysis and molecular dynamics simulation study. Sci. Rep., 5, 2015, 8926.
    • (2015) Sci. Rep. , vol.5 , pp. 8926
    • Lee, H.S.1
  • 35
    • 0035503219 scopus 로고    scopus 로고
    • Cytoplasmic O-glycosylation prevents cell surface transport of E-cadherin during apoptosis
    • 35 Zhu, W., et al. Cytoplasmic O-glycosylation prevents cell surface transport of E-cadherin during apoptosis. EMBO J. 20 (2001), 5999–6007.
    • (2001) EMBO J. , vol.20 , pp. 5999-6007
    • Zhu, W.1
  • 36
    • 84865004391 scopus 로고    scopus 로고
    • Multiple post-translational modifications regulate E-cadherin transport during apoptosis
    • 36 Geng, F., et al. Multiple post-translational modifications regulate E-cadherin transport during apoptosis. J. Cell Sci. 125 (2012), 2615–2625.
    • (2012) J. Cell Sci. , vol.125 , pp. 2615-2625
    • Geng, F.1
  • 37
    • 84883642451 scopus 로고    scopus 로고
    • Glycan structures contain information for the spatial arrangement of glycoproteins in the plasma membrane
    • 37 Hall, M.K., et al. Glycan structures contain information for the spatial arrangement of glycoproteins in the plasma membrane. PLoS ONE, 8, 2013, e75013.
    • (2013) PLoS ONE , vol.8 , pp. e75013
    • Hall, M.K.1
  • 38
    • 84908667025 scopus 로고    scopus 로고
    • Cell surface N-glycans influence the level of functional E-cadherin at the cell–cell border
    • 38 Hall, M.K., et al. Cell surface N-glycans influence the level of functional E-cadherin at the cell–cell border. FEBS Open Bio. 4 (2014), 892–897.
    • (2014) FEBS Open Bio. , vol.4 , pp. 892-897
    • Hall, M.K.1
  • 39
    • 84973601957 scopus 로고    scopus 로고
    • Predominant expression of hybrid N-glycans has distinct cellular roles relative to complex and oligomannose N-glycans
    • 39 Hall, M.K., et al. Predominant expression of hybrid N-glycans has distinct cellular roles relative to complex and oligomannose N-glycans. Int. J. Mol. Sci., 17, 2016, 925.
    • (2016) Int. J. Mol. Sci. , vol.17 , pp. 925
    • Hall, M.K.1
  • 40
    • 84962250130 scopus 로고    scopus 로고
    • Kinetic leasurements reveal enhanced protein-protein interactions at intercellular junctions
    • 40 Shashikanth, N., et al. Kinetic leasurements reveal enhanced protein-protein interactions at intercellular junctions. Sci. Rep., 6, 2016, 23623.
    • (2016) Sci. Rep. , vol.6 , pp. 23623
    • Shashikanth, N.1
  • 41
    • 84864822203 scopus 로고    scopus 로고
    • N-Glycosylation alters cadherin-mediated intercellular binding kinetics
    • 41 Langer, M.D., et al. N-Glycosylation alters cadherin-mediated intercellular binding kinetics. J. Cell Sci. 125 (2012), 2478–2485.
    • (2012) J. Cell Sci. , vol.125 , pp. 2478-2485
    • Langer, M.D.1
  • 42
    • 71749112448 scopus 로고    scopus 로고
    • Regulation of homotypic cell–cell adhesion by branched N-glycosylation of N-cadherin extracellular EC2 and EC3 domains
    • 42 Guo, H-B., et al. Regulation of homotypic cell–cell adhesion by branched N-glycosylation of N-cadherin extracellular EC2 and EC3 domains. J. Biol. Chem. 284 (2009), 34986–34997.
    • (2009) J. Biol. Chem. , vol.284 , pp. 34986-34997
    • Guo, H.-B.1
  • 43
    • 84891368942 scopus 로고    scopus 로고
    • Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins
    • 43 Vester-Christensen, M.B., et al. Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins. Proc. Natl. Acad. Sci. U.S.A. 110 (2013), 21018–21023.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 21018-21023
    • Vester-Christensen, M.B.1
  • 44
    • 84891359272 scopus 로고    scopus 로고
    • O-Mannosylation of cadherins
    • 44 Baenziger, J.U., O-Mannosylation of cadherins. Proc. Natl. Acad. Sci. U.S.A. 110 (2013), 20858–20859.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 20858-20859
    • Baenziger, J.U.1
  • 45
    • 84891363796 scopus 로고    scopus 로고
    • Protein O-mannosylation is crucial for E-cadherin–mediated cell adhesion
    • 45 Lommel, M., et al. Protein O-mannosylation is crucial for E-cadherin–mediated cell adhesion. Proc. Natl. Acad. Sci. U.S.A. 110 (2013), 21024–21029.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 21024-21029
    • Lommel, M.1
  • 46
    • 84887401948 scopus 로고    scopus 로고
    • O-Glycosylation of the non-canonical T-cadherin from rabbit skeletal muscle by single mannose residues
    • 46 Winterhalter, P.R., et al. O-Glycosylation of the non-canonical T-cadherin from rabbit skeletal muscle by single mannose residues. FEBS Lett. 587 (2013), 3715–3721.
    • (2013) FEBS Lett. , vol.587 , pp. 3715-3721
    • Winterhalter, P.R.1
  • 47
    • 79953721653 scopus 로고    scopus 로고
    • Modulation of E-cadherin function and dysfunction by N-glycosylation
    • 47 Pinho, S.S., et al. Modulation of E-cadherin function and dysfunction by N-glycosylation. Cell. Mol. Life. Sci. 68 (2011), 1011–1020.
    • (2011) Cell. Mol. Life. Sci. , vol.68 , pp. 1011-1020
    • Pinho, S.S.1
  • 48
    • 33747377812 scopus 로고    scopus 로고
    • N-Glycosylation affects the molecular organization and stability of E-cadherin junctions
    • 48 Liwosz, A., et al. N-Glycosylation affects the molecular organization and stability of E-cadherin junctions. J. Biol. Chem. 281 (2006), 23138–23149.
    • (2006) J. Biol. Chem. , vol.281 , pp. 23138-23149
    • Liwosz, A.1
  • 49
    • 77953231144 scopus 로고    scopus 로고
    • N-Glycosylation status of E-cadherin controls cytoskeletal dynamics through the organization of distinct β-catenin- and γ-catenin-containing AJs
    • 49 Jamal, B.T., et al. N-Glycosylation status of E-cadherin controls cytoskeletal dynamics through the organization of distinct β-catenin- and γ-catenin-containing AJs. Cell Health Cytoskelet. 2009 (2009), 67–80.
    • (2009) Cell Health Cytoskelet. , vol.2009 , pp. 67-80
    • Jamal, B.T.1
  • 50
    • 77953232964 scopus 로고    scopus 로고
    • Hypoglycosylated E-cadherin promotes the assembly of tight junctions through the recruitment of PP2A to adherens junctions
    • 50 Nita-Lazar, M., et al. Hypoglycosylated E-cadherin promotes the assembly of tight junctions through the recruitment of PP2A to adherens junctions. Exp. Cell Res. 316 (2010), 1871–1884.
    • (2010) Exp. Cell Res. , vol.316 , pp. 1871-1884
    • Nita-Lazar, M.1
  • 51
    • 84923288088 scopus 로고    scopus 로고
    • Glycans and cancer: role of N-Glycans in cancer biomarker, progression and metastasis, and therapeutics
    • R.D. Richard E.B. Lauren Academic Press
    • 51 Taniguchi, N., Kizuka, Y., Glycans and cancer: role of N-Glycans in cancer biomarker, progression and metastasis, and therapeutics. Richard, R.D., Lauren, E.B., (eds.) Advances in Cancer Research, 2015, Academic Press, 11–51.
    • (2015) Advances in Cancer Research , pp. 11-51
    • Taniguchi, N.1    Kizuka, Y.2
  • 52
    • 84899648864 scopus 로고    scopus 로고
    • Decreased core-fucosylation contributes to malignancy in gastric cancer
    • 52 Zhao, Y-P., et al. Decreased core-fucosylation contributes to malignancy in gastric cancer. PLoS ONE, 9, 2014, e94536.
    • (2014) PLoS ONE , vol.9 , pp. e94536
    • Zhao, Y.-P.1
  • 53
    • 84885803283 scopus 로고    scopus 로고
    • The identification and characterization of novel N-glycan-based biomarkers in gastric cancer
    • 53 Liu, L., et al. The identification and characterization of novel N-glycan-based biomarkers in gastric cancer. PLoS ONE, 8, 2013, e77821.
    • (2013) PLoS ONE , vol.8 , pp. e77821
    • Liu, L.1
  • 54
    • 65349145229 scopus 로고    scopus 로고
    • Core fucosylation of E-cadherin enhances cell–cell adhesion in human colon carcinoma WiDr cells
    • 54 Osumi, D., et al. Core fucosylation of E-cadherin enhances cell–cell adhesion in human colon carcinoma WiDr cells. Cancer Sci. 100 (2009), 888–895.
    • (2009) Cancer Sci. , vol.100 , pp. 888-895
    • Osumi, D.1
  • 55
    • 56949098199 scopus 로고    scopus 로고
    • E-Cadherin core fucosylation regulates nuclear β-catenin accumulation in lung cancer cells
    • 55 Hu, P., et al. E-Cadherin core fucosylation regulates nuclear β-catenin accumulation in lung cancer cells. Glycoconj. J. 25 (2008), 843–850.
    • (2008) Glycoconj. J. , vol.25 , pp. 843-850
    • Hu, P.1
  • 56
    • 84960387090 scopus 로고    scopus 로고
    • Posttranslational modification of E-cadherin by core fucosylation regulates Src activation and induces epithelial–mesenchymal transition-like process in lung cancer cells
    • 56 Shao, K., et al. Posttranslational modification of E-cadherin by core fucosylation regulates Src activation and induces epithelial–mesenchymal transition-like process in lung cancer cells. Glycobiology 26 (2016), 142–154.
    • (2016) Glycobiology , vol.26 , pp. 142-154
    • Shao, K.1
  • 57
    • 84862667123 scopus 로고    scopus 로고
    • Development of an AlphaLISA assay to quantify serum core-fucosylated E-cadherin as a metastatic lung adenocarcinoma biomarker
    • 57 Wen, C-L., et al. Development of an AlphaLISA assay to quantify serum core-fucosylated E-cadherin as a metastatic lung adenocarcinoma biomarker. J. Proteomics 75 (2012), 3963–3976.
    • (2012) J. Proteomics , vol.75 , pp. 3963-3976
    • Wen, C.-L.1
  • 58
    • 85012073773 scopus 로고    scopus 로고
    • Enzymes for N-glycan branching and their genetic and nongenetic regulation in cancer
    • 58 Kizuka, Y., Taniguchi, N., Enzymes for N-glycan branching and their genetic and nongenetic regulation in cancer. Biomolecules, 6, 2016, 25.
    • (2016) Biomolecules , vol.6 , pp. 25
    • Kizuka, Y.1    Taniguchi, N.2
  • 59
    • 0030754637 scopus 로고    scopus 로고
    • Transcriptional regulation of N-acetylglucosaminyltransferase V by the src oncogene
    • 59 Buckhaults, P., et al. Transcriptional regulation of N-acetylglucosaminyltransferase V by the src oncogene. J. Biol. Chem. 272 (1997), 19575–19581.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19575-19581
    • Buckhaults, P.1
  • 60
    • 84896726639 scopus 로고    scopus 로고
    • Expression of N-acetylglucosaminyltransferase V in gastric cancer correlates with metastasis and prognosis
    • 60 Huang, B., et al. Expression of N-acetylglucosaminyltransferase V in gastric cancer correlates with metastasis and prognosis. Int. J. Oncol. 44 (2014), 849–857.
    • (2014) Int. J. Oncol. , vol.44 , pp. 849-857
    • Huang, B.1
  • 61
    • 0034069025 scopus 로고    scopus 로고
    • Expression of N-acetylglucosaminyltransferase V in colorectal cancer correlates with metastasis and poor prognosis
    • 61 Murata, K., et al. Expression of N-acetylglucosaminyltransferase V in colorectal cancer correlates with metastasis and poor prognosis. Am. Assoc. Cancer Res. 6 (2000), 1772–1777.
    • (2000) Am. Assoc. Cancer Res. , vol.6 , pp. 1772-1777
    • Murata, K.1
  • 62
    • 49149107798 scopus 로고    scopus 로고
    • + T cells and macrophages
    • + T cells and macrophages. J. Immunol. 180 (2008), 3158–3165.
    • (2008) J. Immunol. , vol.180 , pp. 3158-3165
    • Li, D.1
  • 63
    • 0029021007 scopus 로고
    • Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V
    • 63 Demetriou, M., et al. Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V. J. Cell Biol. 130 (1995), 383–392.
    • (1995) J. Cell Biol. , vol.130 , pp. 383-392
    • Demetriou, M.1
  • 64
    • 78650451823 scopus 로고    scopus 로고
    • Specific posttranslational modification regulates early events in mammary carcinoma formation
    • 64 Guo, H-B., et al. Specific posttranslational modification regulates early events in mammary carcinoma formation. Proc. Natl. Acad. Sci. U.S.A. 107 (2010), 21116–21121.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 21116-21121
    • Guo, H.-B.1
  • 65
    • 84909953198 scopus 로고    scopus 로고
    • min/+ mice through altered Wnt receptor signaling
    • min/+ mice through altered Wnt receptor signaling. J. Biol. Chem. 289 (2014), 31534–31549.
    • (2014) J. Biol. Chem. , vol.289 , pp. 31534-31549
    • Guo, H.1
  • 66
    • 79960838030 scopus 로고    scopus 로고
    • Down-regulation of GnT-V inhibits nasopharyngeal carcinoma cell CNE-2 malignancy in vitro and in vivo
    • 66 Wei, T., et al. Down-regulation of GnT-V inhibits nasopharyngeal carcinoma cell CNE-2 malignancy in vitro and in vivo. Cancer Lett. 309 (2011), 151–161.
    • (2011) Cancer Lett. , vol.309 , pp. 151-161
    • Wei, T.1
  • 67
    • 0034061923 scopus 로고    scopus 로고
    • Suppression of tumor growth and metastasis in Mgat5-deficient mice
    • 67 Granovsky, M., et al. Suppression of tumor growth and metastasis in Mgat5-deficient mice. Nat. Med. 6 (2000), 306–312.
    • (2000) Nat. Med. , vol.6 , pp. 306-312
    • Granovsky, M.1
  • 68
    • 84936774693 scopus 로고    scopus 로고
    • Assembly, organization and regulation of cell-surface receptors by lectin–glycan complexes
    • 68 Elola, M.T., et al. Assembly, organization and regulation of cell-surface receptors by lectin–glycan complexes. Biochem. J. 469 (2015), 1–16.
    • (2015) Biochem. J. , vol.469 , pp. 1-16
    • Elola, M.T.1
  • 69
    • 84935505241 scopus 로고    scopus 로고
    • The galectin lattice at a glance
    • 69 Nabi, I.R., et al. The galectin lattice at a glance. J. Cell Sci. 128 (2015), 2213–2219.
    • (2015) J. Cell Sci. , vol.128 , pp. 2213-2219
    • Nabi, I.R.1
  • 70
    • 67649859659 scopus 로고    scopus 로고
    • The role of N-acetylglucosaminyltransferase III and V in the post-transcriptional modifications of E-cadherin
    • 70 Pinho, S.S., et al. The role of N-acetylglucosaminyltransferase III and V in the post-transcriptional modifications of E-cadherin. Hum. Mol. Genet. 18 (2009), 2599–2608.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 2599-2608
    • Pinho, S.S.1
  • 71
    • 84873589547 scopus 로고    scopus 로고
    • E-Cadherin and adherens-junctions stability in gastric carcinoma: Functional implications of glycosyltransferases involving N-glycan branching biosynthesis, N-acetylglucosaminyltransferases III and V
    • 71 Pinho, S.S., et al. E-Cadherin and adherens-junctions stability in gastric carcinoma: Functional implications of glycosyltransferases involving N-glycan branching biosynthesis, N-acetylglucosaminyltransferases III and V. Biochim. Biophys. Acta (BBA) - Gen. Sub. 1830 (2013), 2690–2700.
    • (2013) Biochim. Biophys. Acta (BBA) - Gen. Sub. , vol.1830 , pp. 2690-2700
    • Pinho, S.S.1
  • 72
    • 84937605601 scopus 로고    scopus 로고
    • Preventing E-cadherin aberrant N-glycosylation at Asn-554 improves its critical function in gastric cancer
    • 72 Carvalho, S., et al. Preventing E-cadherin aberrant N-glycosylation at Asn-554 improves its critical function in gastric cancer. Oncogene 35 (2016), 1619–1631.
    • (2016) Oncogene , vol.35 , pp. 1619-1631
    • Carvalho, S.1
  • 73
    • 85079924139 scopus 로고    scopus 로고
    • E-cadherin glycosylation in cancer. In Glycoscience: Biology and Medicine (Endo, T. eds), Springer Japan
    • 73 Pinho, S.S. and Reis, C.A. (2011) E-cadherin glycosylation in cancer. In Glycoscience: Biology and Medicine (Endo, T. et al. eds), pp. 1-6, Springer Japan.
    • (2011) , pp. 1-6
    • Pinho, S.S.1    Reis, C.A.2
  • 74
    • 0347993082 scopus 로고    scopus 로고
    • N-Acetylglucosaminyltransferase V expression levels regulate cadherin-associated homotypic cell–cell adhesion and intracellular signaling pathways
    • 74 Guo, H-B., et al. N-Acetylglucosaminyltransferase V expression levels regulate cadherin-associated homotypic cell–cell adhesion and intracellular signaling pathways. J. Biol. Chem. 278 (2003), 52412–52424.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52412-52424
    • Guo, H.-B.1
  • 75
    • 39749092710 scopus 로고    scopus 로고
    • N-Glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway
    • 75 Zhao, H., et al. N-Glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway. Acta Biochim. Biophys. Sin. (Shanghai). 40 (2008), 140–148.
    • (2008) Acta Biochim. Biophys. Sin. (Shanghai). , vol.40 , pp. 140-148
    • Zhao, H.1
  • 76
    • 46449101373 scopus 로고    scopus 로고
    • N-Glycosylation affects the adhesive function of E-Cadherin through modifying the composition of adherens junctions (AJs) in human breast carcinoma cell line MDA-MB-435
    • 76 Zhao, H., et al. N-Glycosylation affects the adhesive function of E-Cadherin through modifying the composition of adherens junctions (AJs) in human breast carcinoma cell line MDA-MB-435. J. Cell. Biochem. 104 (2008), 162–175.
    • (2008) J. Cell. Biochem. , vol.104 , pp. 162-175
    • Zhao, H.1
  • 77
    • 84901791985 scopus 로고    scopus 로고
    • Protein N-glycosylation in oral cancer: dysregulated cellular networks among DPAGT1, E-cadherin adhesion and canonical Wnt signaling
    • 77 Varelas, X., et al. Protein N-glycosylation in oral cancer: dysregulated cellular networks among DPAGT1, E-cadherin adhesion and canonical Wnt signaling. Glycobiology 24 (2014), 579–591.
    • (2014) Glycobiology , vol.24 , pp. 579-591
    • Varelas, X.1
  • 78
    • 67650999377 scopus 로고    scopus 로고
    • Overexpression of DPAGT1 leads to aberrant N-glycosylation of E-cadherin and cellular discohesion in oral cancer
    • 78 Nita-Lazar, M., et al. Overexpression of DPAGT1 leads to aberrant N-glycosylation of E-cadherin and cellular discohesion in oral cancer. Cancer Res. 69 (2009), 5673–5680.
    • (2009) Cancer Res. , vol.69 , pp. 5673-5680
    • Nita-Lazar, M.1
  • 79
    • 53849109165 scopus 로고    scopus 로고
    • Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD
    • 79 Zhou, F., et al. Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD. Glycoconj. J. 25 (2008), 727–740.
    • (2008) Glycoconj. J. , vol.25 , pp. 727-740
    • Zhou, F.1
  • 80
    • 84903480443 scopus 로고    scopus 로고
    • Sialic acids sweeten a tumor's life
    • 80 Büll, C., et al. Sialic acids sweeten a tumor's life. Cancer Res. 74 (2014), 3199–3204.
    • (2014) Cancer Res. , vol.74 , pp. 3199-3204
    • Büll, C.1
  • 81
    • 84903589790 scopus 로고    scopus 로고
    • Sialosignaling: sialyltransferases as engines of self-fueling loops in cancer progression
    • 81 Dall'Olio, F., et al. Sialosignaling: sialyltransferases as engines of self-fueling loops in cancer progression. Biochim. Biophys. Acta Gen. Sub. 1840 (2014), 2752–2764.
    • (2014) Biochim. Biophys. Acta Gen. Sub. , vol.1840 , pp. 2752-2764
    • Dall'Olio, F.1
  • 82
    • 0004106191 scopus 로고    scopus 로고
    • Essentials of Glycobiology
    • Cold Spring Harbor Laboratory Press
    • 82 Varki, A., Essentials of Glycobiology. 2009, Cold Spring Harbor Laboratory Press.
    • (2009)
    • Varki, A.1
  • 83
    • 84933675035 scopus 로고    scopus 로고
    • Complexity and diversity of the mammalian sialome revealed by nidovirus virolectins
    • 83 Langereis, M.A., et al. Complexity and diversity of the mammalian sialome revealed by nidovirus virolectins. Cell Rep. 11 (2015), 1966–1978.
    • (2015) Cell Rep. , vol.11 , pp. 1966-1978
    • Langereis, M.A.1
  • 84
    • 68949159937 scopus 로고    scopus 로고
    • Molecular plasticity of E-cadherin and sialyl Lewis X expression, in two comparative models of mammary tumorigenesis
    • 84 Pinho, S.S., et al. Molecular plasticity of E-cadherin and sialyl Lewis X expression, in two comparative models of mammary tumorigenesis. PLoS ONE, 4, 2009, e6636.
    • (2009) PLoS ONE , vol.4 , pp. e6636
    • Pinho, S.S.1
  • 85
    • 0036351383 scopus 로고    scopus 로고
    • Cell surface α2,6-sialylation affects adhesion of breast carcinoma cells
    • 85 Lin, S., et al. Cell surface α2,6-sialylation affects adhesion of breast carcinoma cells. Exp. Cell Res. 276 (2002), 101–110.
    • (2002) Exp. Cell Res. , vol.276 , pp. 101-110
    • Lin, S.1
  • 86
    • 84977578357 scopus 로고    scopus 로고
    • The tumor-associated glycosyltransferase ST6Gal-I regulates stem cell transcription factors and confers a cancer stem cell phenotype
    • 86 Schultz, M.J., et al. The tumor-associated glycosyltransferase ST6Gal-I regulates stem cell transcription factors and confers a cancer stem cell phenotype. Cancer Res. 76 (2016), 3978–3988.
    • (2016) Cancer Res. , vol.76 , pp. 3978-3988
    • Schultz, M.J.1
  • 87
    • 84993660248 scopus 로고    scopus 로고
    • O-Mannosylation and N-glycosylation: two coordinated mechanisms regulating the tumour suppressor functions of E-cadherin in cancer
    • Published online August 12, 2016
    • 87 Carvalho, S., et al. O-Mannosylation and N-glycosylation: two coordinated mechanisms regulating the tumour suppressor functions of E-cadherin in cancer. Oncotarget., 2016, 10.18632/oncotarget.11245 Published online August 12, 2016.
    • (2016) Oncotarget.
    • Carvalho, S.1
  • 88
    • 84877921283 scopus 로고    scopus 로고
    • A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells
    • 88 Jin, F-Z., et al. A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells. Exp. Cell Res. 319 (2013), 1482–1490.
    • (2013) Exp. Cell Res. , vol.319 , pp. 1482-1490
    • Jin, F.-Z.1
  • 89
    • 84920186308 scopus 로고    scopus 로고
    • Aberrant O-GlcNAcylated proteins: new perspectives in breast and colorectal cancer
    • 89 Chaiyawat, P., et al. Aberrant O-GlcNAcylated proteins: new perspectives in breast and colorectal cancer. Front. Endocrinol. (Lausanne)., 5, 2014, 193.
    • (2014) Front. Endocrinol. (Lausanne). , vol.5 , pp. 193
    • Chaiyawat, P.1
  • 90
    • 79951985619 scopus 로고    scopus 로고
    • Core fucosylation and α2-3 sialylation in serum N-glycome is significantly increased in prostate cancer comparing to benign prostate hyperplasia
    • 90 Saldova, R., et al. Core fucosylation and α2-3 sialylation in serum N-glycome is significantly increased in prostate cancer comparing to benign prostate hyperplasia. Glycobiology 21 (2011), 195–205.
    • (2011) Glycobiology , vol.21 , pp. 195-205
    • Saldova, R.1
  • 91
    • 84893271495 scopus 로고    scopus 로고
    • Modification of sialylation mediates the invasive properties and chemosensitivity of human hepatocellular carcinoma
    • 91 Zhao, Y., et al. Modification of sialylation mediates the invasive properties and chemosensitivity of human hepatocellular carcinoma. Mol. Cell. Proteomics 13 (2014), 520–536.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 520-536
    • Zhao, Y.1
  • 92
    • 84888586398 scopus 로고    scopus 로고
    • Increasing the α2,6 sialylation of glycoproteins may contribute to metastatic spread and therapeutic resistance in colorectal cancer
    • 92 Park, J-J., Lee, M., Increasing the α2,6 sialylation of glycoproteins may contribute to metastatic spread and therapeutic resistance in colorectal cancer. Gut. Liver 7 (2013), 629–641.
    • (2013) Gut. Liver , vol.7 , pp. 629-641
    • Park, J.-J.1    Lee, M.2
  • 93
    • 84867965064 scopus 로고    scopus 로고
    • Regulation of the metastatic cell phenotype by sialylated glycans
    • 93 Schultz, M.J., et al. Regulation of the metastatic cell phenotype by sialylated glycans. Cancer Metastasis Rev. 31 (2012), 501–518.
    • (2012) Cancer Metastasis Rev. , vol.31 , pp. 501-518
    • Schultz, M.J.1
  • 94
    • 0037118588 scopus 로고    scopus 로고
    • Cooperative role of E-cadherin and sialyl-Lewis X/A-deficient MUC1 in the passive dissemination of tumor emboli in inflammatory breast carcinoma
    • 94 Alpaugh, M.L., et al. Cooperative role of E-cadherin and sialyl-Lewis X/A-deficient MUC1 in the passive dissemination of tumor emboli in inflammatory breast carcinoma. Oncogene 21 (2002), 3631–3643.
    • (2002) Oncogene , vol.21 , pp. 3631-3643
    • Alpaugh, M.L.1
  • 95
    • 84879165131 scopus 로고    scopus 로고
    • Expression of ST3GAL4 leads to SLe(x) expression and induces c-Met Activation and an invasive phenotype in gastric carcinoma cells
    • 95 Gomes, C., et al. Expression of ST3GAL4 leads to SLe(x) expression and induces c-Met Activation and an invasive phenotype in gastric carcinoma cells. PLoS ONE, 8, 2013, e66737.
    • (2013) PLoS ONE , vol.8 , pp. e66737
    • Gomes, C.1
  • 96
    • 84902337828 scopus 로고    scopus 로고
    • Pancreatic cancer cell glycosylation regulates cell adhesion and invasion through the modulation of α2β1 integrin and E-cadherin function
    • 96 Bassagañas, S., et al. Pancreatic cancer cell glycosylation regulates cell adhesion and invasion through the modulation of α2β1 integrin and E-cadherin function. PLoS ONE, 9, 2014, e98595.
    • (2014) PLoS ONE , vol.9 , pp. e98595
    • Bassagañas, S.1
  • 97
    • 28644451894 scopus 로고    scopus 로고
    • Coexpression of β1,6-N-acetylglucosaminyltransferase V glycoprotein substrates defines aggressive breast cancers with poor outcome
    • 97 Siddiqui, S.F., et al. Coexpression of β1,6-N-acetylglucosaminyltransferase V glycoprotein substrates defines aggressive breast cancers with poor outcome. Cancer Epidemiol. Biomarkers Prev. 14 (2005), 2517–2523.
    • (2005) Cancer Epidemiol. Biomarkers Prev. , vol.14 , pp. 2517-2523
    • Siddiqui, S.F.1
  • 98
    • 84876259688 scopus 로고    scopus 로고
    • Downregulation of the GnT-V gene inhibits metastasis and invasion of BGC823 gastric cancer cells
    • 98 Huang, B., et al. Downregulation of the GnT-V gene inhibits metastasis and invasion of BGC823 gastric cancer cells. Oncol. Rep. 29 (2013), 2392–2400.
    • (2013) Oncol. Rep. , vol.29 , pp. 2392-2400
    • Huang, B.1
  • 99
    • 84875235311 scopus 로고    scopus 로고
    • N-Acetylglucosaminyltransferase V triggers overexpression of MT1-MMP and reinforces the invasive/metastatic potential of cancer cells
    • 99 Lee, J.H., et al. N-Acetylglucosaminyltransferase V triggers overexpression of MT1-MMP and reinforces the invasive/metastatic potential of cancer cells. Biochem. Biophys. Res. Commun. 431 (2013), 658–663.
    • (2013) Biochem. Biophys. Res. Commun. , vol.431 , pp. 658-663
    • Lee, J.H.1
  • 100
    • 39049105125 scopus 로고    scopus 로고
    • Functional proteomics study reveals that N-acetylglucosaminyltransferase V reinforces the invasive/metastatic potential of colon cancer through aberrant glycosylation on tissue inhibitor of metalloproteinase
    • 100 Kim, Y-S., et al. Functional proteomics study reveals that N-acetylglucosaminyltransferase V reinforces the invasive/metastatic potential of colon cancer through aberrant glycosylation on tissue inhibitor of metalloproteinase. Mol. Cell. Proteomics 7 (2008), 1–14.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1-14
    • Kim, Y.-S.1
  • 101
    • 80051500237 scopus 로고    scopus 로고
    • Enhanced epithelial–mesenchymal transition-like phenotype in N-acetylglucosaminyltransferase V transgenic mouse skin promotes wound healing
    • 101 Terao, M., et al. Enhanced epithelial–mesenchymal transition-like phenotype in N-acetylglucosaminyltransferase V transgenic mouse skin promotes wound healing. J. Biol. Chem. 286 (2011), 28303–28311.
    • (2011) J. Biol. Chem. , vol.286 , pp. 28303-28311
    • Terao, M.1
  • 102
    • 0027289374 scopus 로고
    • cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III)
    • 102 Ihara, Y., et al. cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III). J. Biochem. 113 (1993), 692–698.
    • (1993) J. Biochem. , vol.113 , pp. 692-698
    • Ihara, Y.1
  • 103
    • 84961137388 scopus 로고    scopus 로고
    • Atomic visualization of a flipped-back conformation of bisected glycans bound to specific lectins
    • 103 Nagae, M., et al. Atomic visualization of a flipped-back conformation of bisected glycans bound to specific lectins. Sci. Rep., 6, 2016, 22973.
    • (2016) Sci. Rep. , vol.6 , pp. 22973
    • Nagae, M.1
  • 104
    • 81255184311 scopus 로고    scopus 로고
    • Structural diversity and changes in conformational equilibria of biantennary complex-type N-glycans in water revealed by replica-exchange molecular dynamics simulation
    • 104 Re, S., et al. Structural diversity and changes in conformational equilibria of biantennary complex-type N-glycans in water revealed by replica-exchange molecular dynamics simulation. Biophys. J. 101 (2011), L44–L46.
    • (2011) Biophys. J. , vol.101 , pp. L44-L46
    • Re, S.1
  • 105
    • 0032869011 scopus 로고    scopus 로고
    • Implication of N-acetylglucosaminyltransferases III and V in cancer: gene regulation and signaling mechanism
    • 105 Taniguchi, N., et al. Implication of N-acetylglucosaminyltransferases III and V in cancer: gene regulation and signaling mechanism. Biochim. Biophys. Acta Mol. Basis Dis. 1455 (1999), 287–300.
    • (1999) Biochim. Biophys. Acta Mol. Basis Dis. , vol.1455 , pp. 287-300
    • Taniguchi, N.1
  • 106
    • 33845961737 scopus 로고    scopus 로고
    • N-Acetylglucosaminyltransferase III antagonizes the effect of N-acetylglucosaminyltransferase V on α3β1 integrin-mediated cell migration
    • 106 Zhao, Y., et al. N-Acetylglucosaminyltransferase III antagonizes the effect of N-acetylglucosaminyltransferase V on α3β1 integrin-mediated cell migration. J. Biol. Chem. 281 (2006), 32122–32130.
    • (2006) J. Biol. Chem. , vol.281 , pp. 32122-32130
    • Zhao, Y.1
  • 107
    • 77951072143 scopus 로고    scopus 로고
    • The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression
    • 107 Song, Y., et al. The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression. Cancer Res. 70 (2010), 3361–3371.
    • (2010) Cancer Res. , vol.70 , pp. 3361-3371
    • Song, Y.1
  • 108
    • 0029027831 scopus 로고
    • Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection
    • 108 Yoshimura, M., et al. Suppression of lung metastasis of B16 mouse melanoma by N-acetylglucosaminyltransferase III gene transfection. Proc. Natl. Acad. Sci. U.S.A. 92 (1995), 8754–8758.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8754-8758
    • Yoshimura, M.1
  • 109
    • 0035808365 scopus 로고    scopus 로고
    • The addition of bisecting N-acetylglucosamine residues to e-cadherin down-regulates the tyrosine phosphorylation of β-catenin
    • 109 Kitada, T., et al. The addition of bisecting N-acetylglucosamine residues to e-cadherin down-regulates the tyrosine phosphorylation of β-catenin. J. Biol. Chem. 276 (2001), 475–480.
    • (2001) J. Biol. Chem. , vol.276 , pp. 475-480
    • Kitada, T.1
  • 110
    • 0029933659 scopus 로고    scopus 로고
    • Aberrant glycosylation of E-cadherin enhances cell–cell binding to suppress metastasis
    • 110 Yoshimura, M., et al. Aberrant glycosylation of E-cadherin enhances cell–cell binding to suppress metastasis. J. Biol. Chem. 271 (1996), 13811–13815.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13811-13815
    • Yoshimura, M.1
  • 111
    • 50449107493 scopus 로고    scopus 로고
    • N-Acetylglucosaminyltransferase III expression is regulated by cell–cell adhesion via the E-cadherin–catenin–actin complex
    • 111 Akama, R., et al. N-Acetylglucosaminyltransferase III expression is regulated by cell–cell adhesion via the E-cadherin–catenin–actin complex. Proteomics 8 (2008), 3221–3228.
    • (2008) Proteomics , vol.8 , pp. 3221-3228
    • Akama, R.1
  • 112
    • 33744958178 scopus 로고    scopus 로고
    • Cell–cell interaction-dependent regulation of N-acetylglucosaminyltransferase III and the bisected N-glycans in GE11 epithelial cells: involvement of e-cadherin-mediated cell adhesion
    • 112 Iijima, J., et al. Cell–cell interaction-dependent regulation of N-acetylglucosaminyltransferase III and the bisected N-glycans in GE11 epithelial cells: involvement of e-cadherin-mediated cell adhesion. J. Biol. Chem. 281 (2006), 13038–13046.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13038-13046
    • Iijima, J.1
  • 113
    • 79953006880 scopus 로고    scopus 로고
    • Wnt/β-catenin signaling down-regulates N-acetylglucosaminyltransferase III Expression: the implications of two mutually exclusive pathways for regulation
    • 113 Xu, Q., et al. Wnt/β-catenin signaling down-regulates N-acetylglucosaminyltransferase III Expression: the implications of two mutually exclusive pathways for regulation. J. Biol. Chem. 286 (2011), 4310–4318.
    • (2011) J. Biol. Chem. , vol.286 , pp. 4310-4318
    • Xu, Q.1
  • 114
    • 84860879220 scopus 로고    scopus 로고
    • Roles of N-acetylglucosaminyltransferase III in epithelial-to-Mesenchymal transition induced by transforming growth factor β1 (TGF-β1) in epithelial cell lines
    • 114 Xu, Q., et al. Roles of N-acetylglucosaminyltransferase III in epithelial-to-Mesenchymal transition induced by transforming growth factor β1 (TGF-β1) in epithelial cell lines. J. Biol. Chem. 287 (2012), 16563–16574.
    • (2012) J. Biol. Chem. , vol.287 , pp. 16563-16574
    • Xu, Q.1
  • 115
    • 84858138360 scopus 로고    scopus 로고
    • Loss and recovery of Mgat3 and GnT-III mediated E-cadherin N-glycosylation is a mechanism involved in epithelial–mesenchymal–Epithelial Transitions
    • 115 Pinho, S.S., et al. Loss and recovery of Mgat3 and GnT-III mediated E-cadherin N-glycosylation is a mechanism involved in epithelial–mesenchymal–Epithelial Transitions. PLoS ONE, 7, 2012, e33191.
    • (2012) PLoS ONE , vol.7 , pp. e33191
    • Pinho, S.S.1
  • 116
    • 84925968868 scopus 로고    scopus 로고
    • Pragmatic issues in biomarker evaluation for targeted therapies in cancer
    • 116 de Gramont, A., et al. Pragmatic issues in biomarker evaluation for targeted therapies in cancer. Nat. Rev. Clin. Oncol. 12 (2015), 197–212.
    • (2015) Nat. Rev. Clin. Oncol. , vol.12 , pp. 197-212
    • de Gramont, A.1
  • 117
    • 84921774175 scopus 로고    scopus 로고
    • Familial gastric cancer: genetic susceptibility, pathology, and implications for management. Lancet Oncol. 16, e60-70.
    • 117 Oliveira, C. et al. Familial gastric cancer: genetic susceptibility, pathology, and implications for management. Lancet Oncol. 16, e60-70.
    • Oliveira, C.1
  • 118
    • 84971669845 scopus 로고    scopus 로고
    • Lobular breast cancer: clinical, molecular and morphological characteristics
    • 118 Christgen, M., et al. Lobular breast cancer: clinical, molecular and morphological characteristics. Pathol. Res. Pract. 212 (2016), 583–597.
    • (2016) Pathol. Res. Pract. , vol.212 , pp. 583-597
    • Christgen, M.1
  • 119
    • 79551505279 scopus 로고    scopus 로고
    • Soluble E-cadherin as a serum biomarker candidate: Elevated levels in patients with late-stage colorectal carcinoma and FAP
    • 119 Weiß, J.V., et al. Soluble E-cadherin as a serum biomarker candidate: Elevated levels in patients with late-stage colorectal carcinoma and FAP. Int. J. Cancer 128 (2011), 1384–1392.
    • (2011) Int. J. Cancer , vol.128 , pp. 1384-1392
    • Weiß, J.V.1
  • 120
    • 84971367761 scopus 로고    scopus 로고
    • Quantification of topological features in cell meshes to explore E-cadherin dysfunction
    • 120 Mestre, T., et al. Quantification of topological features in cell meshes to explore E-cadherin dysfunction. Sci. Rep., 6, 2016, 25101.
    • (2016) Sci. Rep. , vol.6 , pp. 25101
    • Mestre, T.1
  • 121
    • 0346963104 scopus 로고    scopus 로고
    • The role of an 80 kDa fragment of E-cadherin in the metastatic progression of prostate cancer
    • 121 Kuefer, R., et al. The role of an 80 kDa fragment of E-cadherin in the metastatic progression of prostate cancer. Am. Assoc. Cancer Res. 9 (2003), 6447–6452.
    • (2003) Am. Assoc. Cancer Res. , vol.9 , pp. 6447-6452
    • Kuefer, R.1
  • 122
    • 0035018890 scopus 로고    scopus 로고
    • Soluble E-cadherin is a valid prognostic marker in gastric carcinoma
    • 122 Chan, A., et al. Soluble E-cadherin is a valid prognostic marker in gastric carcinoma. Gut 48 (2001), 808–811.
    • (2001) Gut , vol.48 , pp. 808-811
    • Chan, A.1
  • 123
    • 84973667748 scopus 로고    scopus 로고
    • The promise of protein glycosylation for personalised medicine
    • 123 Almeida, A., Kolarich, D., The promise of protein glycosylation for personalised medicine. Biochim. Biophys. Acta Gen. Sub. 1860 (2016), 1583–1595.
    • (2016) Biochim. Biophys. Acta Gen. Sub. , vol.1860 , pp. 1583-1595
    • Almeida, A.1    Kolarich, D.2
  • 124
    • 84985993219 scopus 로고    scopus 로고
    • Mass spectrometric quantification of N-linked glycans by reference to exogenous standards
    • Published online July 19, 2016
    • 124 Mehta, N., et al. Mass spectrometric quantification of N-linked glycans by reference to exogenous standards. J. Proteome Res., 2016, 10.1021/acs.jproteome.6b00132 Published online July 19, 2016.
    • (2016) J. Proteome Res.
    • Mehta, N.1
  • 125
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: glycans as novel therapeutic targets
    • 125 Fuster, M.M., Esko, J.D., The sweet and sour of cancer: glycans as novel therapeutic targets. Nat. Rev. Cancer 5 (2005), 526–542.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 126
    • 84862238705 scopus 로고    scopus 로고
    • Determination of site-specific glycan heterogeneity on glycoproteins
    • 126 Kolarich, D., et al. Determination of site-specific glycan heterogeneity on glycoproteins. Nat. Protocols 7 (2012), 1285–1298.
    • (2012) Nat. Protocols , vol.7 , pp. 1285-1298
    • Kolarich, D.1
  • 127
    • 77957786881 scopus 로고    scopus 로고
    • Glycoprotein analysis using protein microarrays and mass spectrometry
    • 127 Patwa, T., et al. Glycoprotein analysis using protein microarrays and mass spectrometry. Mass Spectrom. Rev. 29 (2010), 830–844.
    • (2010) Mass Spectrom. Rev. , vol.29 , pp. 830-844
    • Patwa, T.1
  • 128
    • 84962582275 scopus 로고    scopus 로고
    • Glycomic and sialoproteomic data of gastric carcinoma cells overexpressing ST3GAL4
    • 128 Mereiter, S., et al. Glycomic and sialoproteomic data of gastric carcinoma cells overexpressing ST3GAL4. Data Brief 7 (2016), 814–833.
    • (2016) Data Brief , vol.7 , pp. 814-833
    • Mereiter, S.1
  • 129
    • 84930470850 scopus 로고    scopus 로고
    • Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery
    • 129 Campos, D., et al. Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery. Mol. Cell. Proteomics 14 (2015), 1616–1629.
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 1616-1629
    • Campos, D.1
  • 130
    • 84955258348 scopus 로고    scopus 로고
    • Factors affecting anti-glycan IgG and IgM repertoires in human serum
    • 130 Muthana, S.M., Gildersleeve, J.C., Factors affecting anti-glycan IgG and IgM repertoires in human serum. Sci. Rep., 6, 2016, 19509.
    • (2016) Sci. Rep. , vol.6 , pp. 19509
    • Muthana, S.M.1    Gildersleeve, J.C.2
  • 131
    • 84863798606 scopus 로고    scopus 로고
    • Comparison of printed glycan array, suspension array and ELISA in the detection of human anti-glycan antibodies
    • 131 Pochechueva, T., et al. Comparison of printed glycan array, suspension array and ELISA in the detection of human anti-glycan antibodies. Glycoconj. J. 28 (2011), 507–517.
    • (2011) Glycoconj. J. , vol.28 , pp. 507-517
    • Pochechueva, T.1
  • 132
    • 84880464481 scopus 로고    scopus 로고
    • Glycan microarray screening assay for glycosyltransferase specificities
    • I. Brockhausen Humana Press
    • 132 Peng, W., et al. Glycan microarray screening assay for glycosyltransferase specificities. Brockhausen, I., (eds.) Glycosyltransferases: Methods and Protocols, 2013, Humana Press, 1–14.
    • (2013) Glycosyltransferases: Methods and Protocols , pp. 1-14
    • Peng, W.1
  • 133
    • 79959464070 scopus 로고    scopus 로고
    • Glycan microarrays for decoding the glycome
    • 133 Rillahan, C.D., Paulson, J.C., Glycan microarrays for decoding the glycome. Annu. Rev. Biochem. 80 (2011), 797–823.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 797-823
    • Rillahan, C.D.1    Paulson, J.C.2
  • 134
    • 73649112112 scopus 로고    scopus 로고
    • A strategy for discovery of cancer glyco-biomarkers in serum using newly developed technologies for glycoproteomics
    • 134 Narimatsu, H., et al. A strategy for discovery of cancer glyco-biomarkers in serum using newly developed technologies for glycoproteomics. FEBS J. 277 (2010), 95–105.
    • (2010) FEBS J. , vol.277 , pp. 95-105
    • Narimatsu, H.1
  • 135
    • 84981762367 scopus 로고    scopus 로고
    • Glycomimetics targeting glycosyltransferases: synthetic, computational and structural studies of less-polar conjugates
    • 135 Ghirardello, M., et al. Glycomimetics targeting glycosyltransferases: synthetic, computational and structural studies of less-polar conjugates. Chemistry 22 (2016), 7215–7224.
    • (2016) Chemistry , vol.22 , pp. 7215-7224
    • Ghirardello, M.1
  • 136
    • 78049258456 scopus 로고    scopus 로고
    • Cooperativity between trans and cis interactions in cadherin-mediated junction formation
    • 136 Wu, Y., et al. Cooperativity between trans and cis interactions in cadherin-mediated junction formation. Proc. Natl. Acad. Sci. U.S.A. 107 (2010), 17592–17597.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 17592-17597
    • Wu, Y.1
  • 137
    • 58549115688 scopus 로고    scopus 로고
    • Resolving cadherin interactions and binding cooperativity at the single-molecule level
    • 137 Zhang, Y., et al. Resolving cadherin interactions and binding cooperativity at the single-molecule level. Proc. Natl. Acad. Sci. U.S.A. 106 (2009), 109–114.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 109-114
    • Zhang, Y.1
  • 139
    • 84874279840 scopus 로고    scopus 로고
    • Adherens junction turnover: regulating adhesion through cadherin endocytosis, degradation, and recycling
    • 139 Nanes, B.A., Kowalczyk, A.P., Adherens junction turnover: regulating adhesion through cadherin endocytosis, degradation, and recycling. Subcel. Biochem. 60 (2012), 197–222.
    • (2012) Subcel. Biochem. , vol.60 , pp. 197-222
    • Nanes, B.A.1    Kowalczyk, A.P.2
  • 140
    • 79955508089 scopus 로고    scopus 로고
    • Dynamics of adherens junctions in epithelial establishment, maintenance, and remodeling
    • 140 Baum, B., Georgiou, M., Dynamics of adherens junctions in epithelial establishment, maintenance, and remodeling. J. Cell Biol. 192 (2011), 907–917.
    • (2011) J. Cell Biol. , vol.192 , pp. 907-917
    • Baum, B.1    Georgiou, M.2
  • 141
    • 84892666600 scopus 로고    scopus 로고
    • The challenge and promise of glycomics
    • 141 Cummings, R.D., Pierce, J.M., The challenge and promise of glycomics. Chem. Biol. 21 (2014), 1–15.
    • (2014) Chem. Biol. , vol.21 , pp. 1-15
    • Cummings, R.D.1    Pierce, J.M.2
  • 143
    • 73649139554 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation – putting the pieces together
    • 143 Jensen, P.H., et al. Mucin-type O-glycosylation – putting the pieces together. FEBS J. 277 (2010), 81–94.
    • (2010) FEBS J. , vol.277 , pp. 81-94
    • Jensen, P.H.1
  • 144
    • 84964995177 scopus 로고    scopus 로고
    • Protein O-mannosylation in the early secretory pathway
    • 144 Neubert, P., Strahl, S., Protein O-mannosylation in the early secretory pathway. Curr. Opin. Cell Biol. 41 (2016), 100–108.
    • (2016) Curr. Opin. Cell Biol. , vol.41 , pp. 100-108
    • Neubert, P.1    Strahl, S.2
  • 145
    • 84901036287 scopus 로고    scopus 로고
    • Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates
    • 145 Praissman, J.L., Wells, L., Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates. Biochemistry 53 (2014), 3066–3078.
    • (2014) Biochemistry , vol.53 , pp. 3066-3078
    • Praissman, J.L.1    Wells, L.2
  • 146
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • 146 Ohtsubo, K., Marth, J.D., Glycosylation in cellular mechanisms of health and disease. Cell 126 (2006), 855–867.
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 147
    • 44449153943 scopus 로고    scopus 로고
    • Functional roles of N-glycans in cell signaling and cell adhesion in cancer
    • 147 Zhao, Y-Y., et al. Functional roles of N-glycans in cell signaling and cell adhesion in cancer. Cancer Sci. 99 (2008), 1304–1310.
    • (2008) Cancer Sci. , vol.99 , pp. 1304-1310
    • Zhao, Y.-Y.1
  • 148
    • 67349258025 scopus 로고    scopus 로고
    • Turning ‘sweet’ on immunity: galectin–glycan interactions in immune tolerance and inflammation
    • 148 Rabinovich, G.A., Toscano, M.A., Turning ‘sweet’ on immunity: galectin–glycan interactions in immune tolerance and inflammation. Nat. Rev. Immunol. 9 (2009), 338–352.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 338-352
    • Rabinovich, G.A.1    Toscano, M.A.2
  • 149
    • 84946491906 scopus 로고    scopus 로고
    • Re-wiring regulatory cell networks in immunity by galectin–glycan interactions
    • 149 Blidner, A.G., et al. Re-wiring regulatory cell networks in immunity by galectin–glycan interactions. FEBS Lett. 589 (2015), 3407–3418.
    • (2015) FEBS Lett. , vol.589 , pp. 3407-3418
    • Blidner, A.G.1


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